RQT4_SCHPO
ID RQT4_SCHPO Reviewed; 455 AA.
AC O13855; Q9UTB9;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Uncharacterized protein C1A6.01c;
GN ORFNames=SPAC1A6.01c, SPAC23C4.20c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-380, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Probably functions as part of the RQC trigger (RQT) complex
CC that activates the ribosome quality control (RQC) pathway, a pathway
CC that degrades nascent peptide chains during problematic translation.
CC {ECO:0000250|UniProtKB:P36119}.
CC -!- SUBUNIT: Component of the RQT (ribosome quality control trigger)
CC complex. {ECO:0000250|UniProtKB:P36119}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB16891.1; -; Genomic_DNA.
DR PIR; T38275; T38275.
DR RefSeq; NP_593192.1; NM_001018588.2.
DR AlphaFoldDB; O13855; -.
DR BioGRID; 278893; 22.
DR STRING; 4896.SPAC1A6.01c.1; -.
DR iPTMnet; O13855; -.
DR MaxQB; O13855; -.
DR PaxDb; O13855; -.
DR PRIDE; O13855; -.
DR EnsemblFungi; SPAC1A6.01c.1; SPAC1A6.01c.1:pep; SPAC1A6.01c.
DR GeneID; 2542431; -.
DR KEGG; spo:SPAC1A6.01c; -.
DR PomBase; SPAC1A6.01c; -.
DR VEuPathDB; FungiDB:SPAC1A6.01c; -.
DR eggNOG; KOG2845; Eukaryota.
DR HOGENOM; CLU_622748_0_0_1; -.
DR InParanoid; O13855; -.
DR OMA; AAPNCLN; -.
DR PhylomeDB; O13855; -.
DR PRO; PR:O13855; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0099053; C:activating signal cointegrator 1 complex; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:PomBase.
DR InterPro; IPR039128; TRIP4-like.
DR InterPro; IPR009349; Znf_C2HC5.
DR PANTHER; PTHR12963; PTHR12963; 1.
DR Pfam; PF06221; zf-C2HC5; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..455
FT /note="Uncharacterized protein C1A6.01c"
FT /id="PRO_0000116731"
FT REGION 64..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 455 AA; 50907 MW; 5497C862C5FF1726 CRC64;
MEKWTKENVL KILPVDDESA AMITSTALAV DSSEAAKDYW ISLLGDSAET IEFISDFNQK
RFHSTHSGNS PSIMKNKKNV TPNNNIRQKN TATSSHPSFY IANNKQKGYD EEMYKVNPAS
RNKSQSNNIS SHEKSSKTTK NVSPGVMTSD LIPEKKSVKH NNSSSNRIEG LADIEKAIRQ
IEISQNINKA ERRVCNCQGR KHPLNEAAPN CLNCGKIICI VEGIGPCTFC DNPVISKAQQ
LELIQELKHE GSRLKQAANQ KRKSKTVSSK NNFQRLQNSS LHSIFLDPKQ LEQKAQEAEE
RKNVLLNFDR TSAQRTRIID EAADFDPTSL ASDTWASPAE KALNLVRMQK AMAKKEKKKK
KVLSISLSGK KVVVDQKEAS SESSDEDQDE LDNLTKVEGQ SHSHNPKAPV IRNLPRPIYH
QDLHSSHVAV PESILNKINQ KWSKVQDDDG MPSML
